scholarly journals Role of prolyl hydroxylation in the molecular interactions of collagens

2019 ◽  
Vol 63 (3) ◽  
pp. 325-335 ◽  
Author(s):  
Pekka Rappu ◽  
Antti M. Salo ◽  
Johanna Myllyharju ◽  
Jyrki Heino
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Collagen Structure ◽  
Complex Interplay ◽  
Cell Behaviour ◽  
Qualitative And Quantitative ◽  
Proline Hydroxylation ◽  
Prolyl Hydroxylation ◽  
The Stability

Abstract Co- and post-translational hydroxylation of proline residues is critical for the stability of the triple helical collagen structure. In this review, we summarise the biology of collagen prolyl 4-hydroxylases and collagen prolyl 3-hydroxylases, the enzymes responsible for proline hydroxylation. Furthermore, we describe the potential roles of hydroxyproline residues in the complex interplay between collagens and other proteins, especially integrin and discoidin domain receptor type cell adhesion receptors. Qualitative and quantitative regulation of collagen hydroxylation may have remarkable effects on the properties of the extracellular matrix and consequently on the cell behaviour.

scholarly journals Role of Extracellular Matrix in Development and Cancer Progression

2018 ◽  
Vol 19 (10) ◽  
pp. 3028 ◽  
Author(s):  
Cameron Walker ◽  
Elijah Mojares ◽  
Armando del Río Hernández
Keyword(s):  
Extracellular Matrix ◽  
Cancer Progression ◽  
Chemical Cues ◽  
Control Cell ◽  
Malignant Cell ◽  
Cell Phenotype ◽  
Cell Behaviour ◽  
Biophysical Forces ◽  
Key Drivers

The immense diversity of extracellular matrix (ECM) proteins confers distinct biochemical and biophysical properties that influence cell phenotype. The ECM is highly dynamic as it is constantly deposited, remodelled, and degraded during development until maturity to maintain tissue homeostasis. The ECM’s composition and organization are spatiotemporally regulated to control cell behaviour and differentiation, but dysregulation of ECM dynamics leads to the development of diseases such as cancer. The chemical cues presented by the ECM have been appreciated as key drivers for both development and cancer progression. However, the mechanical forces present due to the ECM have been largely ignored but recently recognized to play critical roles in disease progression and malignant cell behaviour. Here, we review the ways in which biophysical forces of the microenvironment influence biochemical regulation and cell phenotype during key stages of human development and cancer progression.

The role of the physicochemical environment in determining disc cell behaviour

2002 ◽  
Vol 30 (6) ◽  
pp. 858-863 ◽  
Author(s):  
J. P. G. Urban
Keyword(s):  
Extracellular Matrix ◽  
Ionic Composition ◽  
Cell Types ◽  
Mechanical Forces ◽  
Dense Matrix ◽  
Cellular Activity ◽  
High Concentration ◽  
Cell Behaviour ◽  
Disc Cells

The cells of the intervertebral disc exist in an unusual environment. They are embedded in a dense matrix containing a high concentration of aggrecan whose fixed negative charges regulate the extracellular ionic composition and osmolarity; both extracellular cation concentrations and osmolarity are considerably higher than those experienced by most cell types. The disc also is avascular. Oxygen levels in the centre of the nucleus, where cells may be 6–8 mm from the blood supply, are very low. Since metabolism is mainly by glycolysis, lactic acid is produced at high rates and hence the pH is acidic. Finally, the disc is subjected to mechanical forces at all times; these vary with posture and activity. In particular, because the disc is under low loads during rest and high loads during the day's activities, it loses and regains around 25% of its fluid over a diurnal cycle with consequent changes to the concentrations of extracellular matrix macromolecules and ions and hence extracellular osmolality. Here we will briefly review these factors and discuss the influence of changes in the physicochemical environment on cellular activity, in particular on the rate at which disc cells synthesize and degrade matrix macro-molecules.

Platelets enhance CD4+ lymphocyte adhesion to extracellular matrix under flow conditions: Role of platelet aggregation, integrins, and non-integrin receptors

2006 ◽  
Vol 95 (05) ◽  
pp. 815-821 ◽  
Author(s):  
Yuri Vitkovsky ◽  
Grigory Brill ◽  
Alexander Koltakov ◽  
Nahid Farzam ◽  
David Varon ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
T Cells ◽  
Cell Adhesion ◽  
Platelet Aggregation ◽  
T Cell ◽  
Static Condition ◽  
Flow Conditions ◽  
Lymphocyte Adhesion ◽  
Cd4 Lymphocyte

SummaryThe purpose of this study was to examine the role of platelets in CD4+ T lymphocyte adhesion to subendothelial extracellular matrix (ECM). Herpesvirus saimiri (HVS)-infected CD4+ T cells were incubated on ECM. An image analysis was used to evaluate T cell adhesion. Under static condition, T cell activation with 4-α-Phorbol 12-myristate 13-acetate (PMA) resulted in a 2.6-fold increase in cell adhesion. However, adhesion was not affected by platelets. In contrast, under flow (200s−1), platelets markedly enhanced both resting and PMA-activatedT cell adhesion (33- and 48-fold), forming lymphocyte-platelet co-aggregates that contain approximately 90% of the adherent T cells. Abrogation of platelet aggregation with tirofiban inhibited formation of platelet-T cell co-aggregates under flow and reduced T cell adhesion by 74%. Separate and combined blockade of CD40L and P-selectin glycoprotein-1 (PSGL-1) on PMA-activated lymphocytes reduced adhesion under flow in the presence of platelets by 28%, 33%, and 55%, respectively. Blockade of β1-integrins decreased adhesion under both static and flow conditions (by 35% and 44%, respectively), while blockade of β2-integrin reduced adhesion only under static condition (by 23%). A similar adhesion pattern was observed using CD4+ T cells isolated from normal donor peripheral blood. In conclusion, platelets support CD4+ lymphocyte adhesion to ECM under flow by formation of heterotypic platelet-lymphocyte co-aggregates involving αIIbβ3 integrin and β1-related integrins, as well as CD40L and PSGL-1.

scholarly journals The role of spectrin in cell adhesion and cell–cell contact

2019 ◽  
Vol 244 (15) ◽  
pp. 1303-1312 ◽  
Author(s):  
Beata Machnicka ◽  
Renata Grochowalska ◽  
Dżamila M Bogusławska ◽  
Aleksander F Sikorski
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Biology ◽  
Membrane Integrity ◽  
Cell Contact ◽  
Surface Activities ◽  
New Findings ◽  
Cell Cell

Spectrins are proteins that are responsible for many aspects of cell function and adaptation to changing environments. Primarily the spectrin-based membrane skeleton maintains cell membrane integrity and its mechanical properties, together with the cytoskeletal network a support cell shape. The occurrence of a variety of spectrin isoforms in diverse cellular environments indicates that it is a multifunctional protein involved in numerous physiological pathways. Participation of spectrin in cell–cell and cell–extracellular matrix adhesion and formation of dynamic plasma membrane protrusions and associated signaling events is a subject of interest for researchers in the fields of cell biology and molecular medicine. In this mini-review, we focus on data concerning the role of spectrins in cell surface activities such as adhesion, cell–cell contact, and invadosome formation. We discuss data on different adhesion proteins that directly or indirectly interact with spectrin repeats. New findings support the involvement of spectrin in cell adhesion and spreading, formation of lamellipodia, and also the participation in morphogenetic processes, such as eye development, oogenesis, and angiogenesis. Here, we review the role of spectrin in cell adhesion and cell–cell contact.Impact statementThis article reviews properties of spectrins as a group of proteins involved in cell surface activities such as, adhesion and cell–cell contact, and their contribution to morphogenesis. We show a new area of research and discuss the involvement of spectrin in regulation of cell–cell contact leading to immunological synapse formation and in shaping synapse architecture during myoblast fusion. Data indicate involvement of spectrins in adhesion and cell–cell or cell–extracellular matrix interactions and therefore in signaling pathways. There is evidence of spectrin’s contribution to the processes of morphogenesis which are connected to its interactions with adhesion molecules, membrane proteins (and perhaps lipids), and actin. Our aim was to highlight the essential role of spectrin in cell–cell contact and cell adhesion.

Regulation of hemidesmosome dynamics and cell signaling by integrin α6β4

2021 ◽  
Vol 134 (18) ◽  
Author(s):  
Lisa te Molder ◽  
Jose M. de Pereda ◽  
Arnoud Sonnenberg
Keyword(s):  
Signal Transduction ◽  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Epithelial Cells ◽  
Basement Membrane ◽  
Molecular Mechanisms ◽  
Vital Role ◽  
Cellular Processes ◽  
Integrin Α6β4

ABSTRACT Hemidesmosomes (HDs) are specialized multiprotein complexes that connect the keratin cytoskeleton of epithelial cells to the extracellular matrix (ECM). In the skin, these complexes provide stable adhesion of basal keratinocytes to the underlying basement membrane. Integrin α6β4 is a receptor for laminins and plays a vital role in mediating cell adhesion by initiating the assembly of HDs. In addition, α6β4 has been implicated in signal transduction events that regulate diverse cellular processes, including proliferation and survival. In this Review, we detail the role of α6β4 in HD assembly and beyond, and we discuss the molecular mechanisms that regulate its function.

The Role of Cell Adhesion, Cell Junctions, and Extracellular Matrix in Development and Carcinogenesis

2013 ◽  
pp. 13-49 ◽  
Author(s):  
Anderson K. Santos ◽  
Fernanda M. P. Tonelli ◽  
Daniel A. F. Silva ◽  
Kátia N. Gomes ◽  
Luiz O. Ladeira ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Cell Junctions

scholarly journals Collagen – structure, function and distribution in orodental tissues

2020 ◽  
Vol 2 ◽  
pp. 134-139
Author(s):  
Zaneta D’souza ◽  
Tabita Joy Chettiankandy ◽  
Manisha S. Ahire (Sardar) ◽  
Arush Thakur ◽  
Sarang G. Sonawane ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Structure Function ◽  
Large Family ◽  
The Body ◽  
Collagen Structure ◽  
Basic Framework ◽  
Helical Proteins ◽  
And Function

Collagens are a large family of triple helical proteins which are found extensively throughout the body. They form the basic framework of the extracellular matrix providing support and form to cells and tissues. They are important for various functions such as angiogenesis, morphogenesis, cell adhesion, repair, and regeneration. In this article, we have focused our discussion to the structure, the synthesis, and the degradation of collagen followed by its distribution and function in various oral tissues.

scholarly journals A Scoping Review of the Role of Metalloproteinases in the Pathogenesis of Autoimmune Pemphigus and Pemphigoid

Biomolecules ◽  
2021 ◽  
Vol 11 (10) ◽  
pp. 1506
Author(s):  
Nicola Cirillo ◽  
Stephen S. Prime
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Cell Adhesion Molecules ◽  
Pemphigus Vulgaris ◽  
Experimental Models ◽  
National Library ◽  
Blister Formation ◽  
Life Threatening ◽  
A Disintegrin And Metalloproteinase

Pemphigus and pemphigoid diseases are potentially life-threatening autoimmune blistering disorders that are characterized by intraepithelial and subepithelial blister formation, respectively. In both disease groups, skin and/or mucosal blistering develop as a result of a disruption of intercellular adhesion (pemphigus) and cell-extracellular matrix (ECM) adhesion (pemphigoid). Given that metalloproteinases can target cell adhesion molecules, the purpose of the present study was to investigate the role of these enzymes in the pathogenesis of these bullous dermatoses. Studies examining MMPs (matrix metalloproteinases) and the ADAM (a disintegrin and metalloproteinase) family of proteases in pemphigus and pemphigoid were selected from articles published in the repository of the National Library of Medicine (MEDLINE/PubMed) and bioRxiv. Multiple phases of screening were conducted, and relevant data were extracted and tabulated, with 29 articles included in the final qualitative analysis. The majority of the literature investigated the role of specific components of the MMP family primarily in bullous pemphigoid (BP) whereas studies that focused on pemphigus were rarer. The most commonly studied metalloproteinase was MMP-9 followed by MMP-2; other MMPs included MMP-1, MMP-3, MMP-8, MMP-12 and MMP-13. Molecules related to MMPs were also included, namely, ADAM5, 8, 10, 15, 17, together with TIMP-1 and TIMP-3. The results demonstrated that ADAM10 and MMP-9 activity is necessary for blister formation in experimental models of pemphigus vulgaris (PV) and BP, respectively. The data linking MMPs to the pathogenesis of experimental BP were relatively strong but the evidence for involvement of metalloproteinases in PV was more tentative. These molecules represent potential candidates for the development of mechanism-based treatments of these blistering diseases.

A novel role for alpha 3 beta 1 integrins in extracellular matrix assembly

1995 ◽  
Vol 108 (6) ◽  
pp. 2511-2523 ◽  
Author(s):  
C. Wu ◽  
A.E. Chung ◽  
J.A. McDonald
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Binding Activity ◽  
Integrin Subunit ◽  
Pericellular Matrix ◽  
Matrix Assembly ◽  
Amino Terminal ◽  
Beta 1 Integrin ◽  
Fibronectin Deposition

To study the biological role of alpha 3 beta 1 integrins in cell adhesion, migration, and in the deposition of extracellular matrix, we stably expressed the human alpha 3 integrin subunit in the alpha 4, alpha 5 integrin deficient CHO cell line B2. The expression of alpha 3 beta 1 integrins enhanced cell adhesion on entactin (also known as nidogen), but not on fibronectin. Using recombinant GST-fusion proteins that span the entire length of the entactin molecule, we located cell adhesive activity to the G2 domain of entactin. These results suggest that the alpha 3 beta 1 integrin functions as an adhesion receptor interacting with the G2 domain of entactin. On the other hand, the expression of alpha 3 beta 1 integrins did not confer the ability to migrate on entactin. Strikingly, the expression of alpha 3 beta 1 dramatically increased the deposition of entactin and fibronectin into the pericellular matrix. This was accompanied by increased binding activity of the 29 kDa amino-terminal domain of fibronectin. Thus, similar to alpha 5 beta 1 integrins, alpha 3 beta 1 integrins can play an important role in modulating the assembly of pericellular matrices. However, unlike fibronectin deposition supported by alpha 5 beta 1, alpha 3 beta 1 supported fibronectin deposition into pericellular matrix was not inhibited by antibodies binding to the RGD containing cell adhesion domain of fibronectin, demonstrating that the two processes are mechanistically distinct. The role of alpha 3 beta 1 in pericellular matrix assembly potentially implicates this receptor in the assembly and/or recognition of entactin-containing pericellular matrices, an observation consistent with its apparent role in the renal glomerulus of the mammalian kidney.

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